Dataset Information
Human coagulation factor VIII domain-specific recombinant polypeptide expression.
Ontology highlight
ABSTRACT: Background
Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners.Methods
To determine F8 domain-specific functions during blood coagulation, the FVIII domains A1, A2, A3, and C were cloned from Hep3B hepatocytes. Domain-specific recombinant polypeptides were glutathione S-transferase (GST)- or polyhistidine (His)-tagged, over-expressed in bacteria, and purified by specific affinity chromatography.Results
Recombinant polypeptides of predicted sizes were obtained. The GST-tagged A2 polypeptide interacted with coagulation factor IX, which is known to bind the A2 domain of activated FVIII.Conclusion
Recombinant, domain-specific polypeptides are useful tools to study the domain-specific functions of FVIII during the coagulation process, and they may be used for production of domain-specific antibodies.
SUBMITTER: Choi SJ
PROVIDER: S-EPMC4486152 | biostudies-literature | 2015 Jun
REPOSITORIES: biostudies-literature
Publications
Human coagulation factor VIII domain-specific recombinant polypeptide expression.
Blood research 20150625 2
<h4>Background</h4>Hemophilia A is caused by heterogeneous mutations in F8. Coagulation factor VIII (FVIII), the product of F8, is composed of multiple domains designated A1-A2-B-A3-C1-C2. FVIII is known to interact with diverse proteins, and this characteristic may be important for hemostasis. However, little is known about domain-specific functions or their specific binding partners.<h4>Methods</h4>To determine F8 domain-specific functions during blood coagulation, the FVIII domains A1, A2, A3 ...[more]